Amidophosphoribosyltransferase (P0AG16)

Identification
Name:Amidophosphoribosyltransferase
Synonyms:
  • ATase
  • Glutamine phosphoribosylpyrophosphate amidotransferase
  • GPATase
Gene Name:purF
Enzyme Class:
Biological Properties
General Function:Involved in amidophosphoribosyltransferase activity
Specific Function:5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H(2)O
Cellular Location:Not Available
SMPDB Pathways:
  • Thiamin diphosphate biosynthesis PW002028
  • purine nucleotides de novo biosynthesis PW000910
  • purine nucleotides de novo biosynthesis 1435709748 PW000960
  • purine nucleotides de novo biosynthesis 2 PW002033
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0L-Glutamine + 1.0Water + 1.0Phosphoribosyl pyrophosphate ↔ 1.0L-Glutamate + 1.0Pyrophosphate + 1.05-Phosphoribosylamine
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.05-Phosphoribosylamine + 1.0Pyrophosphate + 1.0L-Glutamate ↔ 1.0L-Glutamine + 1.0Phosphoribosyl pyrophosphate + 1.0Water
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb ← 1.0Thumb+1.0Thumb+1.0Thumb
1.05-Phosphoribosylamine + 1.0Pyrophosphate + 1.0L-Glutamate ← 1.0Phosphoribosyl pyrophosphate + 1.0L-Glutamine + 1.0Water
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.05-Phosphoribosylamine+1.0L-Glutamic acid+1.0Pyrophosphate+1.0Thumb+1.0Thumb
1.0Phosphoribosyl pyrophosphate + 1.0Water + 1.0L-Glutamine → 1.05-Phosphoribosylamine + 1.0L-Glutamic acid + 1.0Pyrophosphate + 1.05-Phosphoribosylamine + 1.0L-Glutamate
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0L-Glutamine + 1.0Water + 1.0Phosphoribosyl pyrophosphate ↔ 1.0L-Glutamate + 1.0Pyrophosphate + 1.05-Phosphoribosylamine
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb ← 1.0Thumb+1.0Thumb+1.0Thumb
1.05-Phosphoribosylamine + 1.0Pyrophosphate + 1.0L-Glutamate ← 1.0Phosphoribosyl pyrophosphate + 1.0L-Glutamine + 1.0Water
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.05-Phosphoribosylamine + 1.0Pyrophosphate + 1.0L-Glutamate → 1.0L-Glutamine + 1.0Phosphoribosyl pyrophosphate + 1.0Water
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB011285-PhosphoribosylamineMetaboCard
ECMDB00148L-GlutamateMetaboCard
ECMDB00641L-GlutamineMetaboCard
ECMDB00280Phosphoribosyl pyrophosphateMetaboCard
ECMDB04142PyrophosphateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
amidophosphoribosyltransferase activity
catalytic activity
transferase activity
transferase activity, transferring glycosyl groups
transferase activity, transferring pentosyl groups
Process
cellular aromatic compound metabolic process
cellular metabolic process
cellular nitrogen compound metabolic process
metabolic process
nitrogen compound metabolic process
nucleobase metabolic process
nucleobase, nucleoside and nucleotide metabolic process
nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
nucleoside metabolic process
purine base biosynthetic process
purine base metabolic process
Gene Properties
Blattner:b2312
Gene OrientationCounterclockwise
Centisome Percentage:52.30
Left Sequence End2426743
Right Sequence End2428260
Gene Sequence:
>1518 bp
ATGGCACAGATTGATTTCCGAAAAAAAATAAACTGGCATCGTCGTTACCGTTCACCGCAG
GGCGTTAAAACCGAACATGAGATCCTGCGGATCTTCGAGAGCGATCGCGGGCGTATCATC
AACTCTCCGGCAATTCGTCGTCTGCAACAAAAGACCCAGGTTTTTCCACTGGAGCGCAAT
GCCGCCGTGCGCACGCGTCTTACCCACTCGATGGAAGTCCAGCAGGTGGGGCGCTACATC
GCCAAAGAAATTTTAAGCCGTCTGAAAGAGCTTAAATTACTGGAAGCATACGGCCTGGAT
GAACTGACCGGTCCCTTTGAAAGCATTGTTGAGATGTCATGCCTGATGCACGATATCGGC
AATCCGCCGTTTGGTCATTTTGGCGAAGCGGCGATAAATGACTGGTTTCGCCAACGTTTG
CACCCGGAAGATGCCGAAAGCCAGCCTCTGACTGACGATCGCTGCAGCGTGGCGGCACTA
CGTTTACGGGACGGGGAAGAACCGCTTAACGAGCTGCGGCGCAAGATTCGTCAGGACTTA
TGTCATTTTGAGGGGAATGCACAAGGCATTCGCCTGGTGCATACATTGATGCGGATGAAT
CTCACCTGGGCACAGGTTGGCGGTATTTTAAAATATACCCGTCCGGCGTGGTGGCGTGGC
GAAACGCCTGAGACACATCACTATTTAATGAAAAAGCCGGGTTATTATCTTTCTGAAGAA
GCCTATATTGCCCGGTTGCGTAAAGAACTTAATTTGGCGCTTTACAGTCGTTTTCCATTA
ACGTGGATTATGGAAGCTGCCGACGACATCTCCTATTGTGTGGCAGACCTTGAAGATGCG
GTAGAGAAAAGAATATTTACCGTTGAGCAGCTTTATCATCATTTGCACGAAGCGTGGGGC
CAGCATGAGAAAGGTTCGCTCTTTTCGCTGGTGGTTGAAAATGCCTGGGAAAAATCACGC
TCAAATAGTTTAAGCCGCAGTACGGAAGATCAGTTTTTTATGTATTTACGGGTAAACACC
CTAAATAAACTGGTACCCTACGCGGCACAACGATTTATTGATAATCTGCCTGCGATTTTC
GCCGGAACGTTTAATCATGCATTATTGGAAGATGCCAGCGAATGCAGCGATCTTCTTAAG
CTATATAAAAATGTCGCTGTAAAACATGTGTTTAGCCATCCAGATGTCGAGCGGCTTGAA
TTGCAGGGCTATCGGGTCATTAGCGGATTATTAGAGATTTATCGTCCTTTATTAAGCCTG
TCGTTATCAGACTTTACTGAACTGGTAGAAAAAGAACGGGTGAAACGTTTCCCTATTGAA
TCGCGCTTATTCCACAAACTCTCGACGCGCCATCGGCTGGCCTATGTCGAGGCTGTCAGT
AAATTACCGTCAGATTCTCCTGAGTTTCCGCTATGGGAATATTATTACCGTTGCCGCCTG
CTGCAGGATTATATCAGCGGTATGACCGACCTCTATGCGTGGGATGAATACCGACGTCTG
ATGGCCGTAGAACAATAA
Protein Properties
Pfam Domain Function:
Protein Residues:505
Protein Molecular Weight:56488
Protein Theoretical pI:5
PDB File:1ECG
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Amidophosphoribosyltransferase
MCGIVGIAGVMPVNQSIYDALTVLQHRGQDAAGIITIDANNCFRLRKANGLVSDVFEARH
MQRLQGNMGIGHVRYPTAGSSSASEAQPFYVNSPYGITLAHNGNLTNAHELRKKLFEEKR
RHINTTSDSEILLNIFASELDNFRHYPLEADNIFAAIAATNRLIRGAYACVAMIIGHGMV
AFRDPNGIRPLVLGKRDIDENRTEYMVASESVALDTLGFDFLRDVAPGEAIYITEEGQLF
TRQCADNPVSNPCLFEYVYFARPDSFIDKISVYSARVNMGTKLGEKIAREWEDLDIDVVI
PIPETSCDIALEIARILGKPYRQGFVKNRYVGRTFIMPGQQLRRKSVRRKLNANRAEFRD
KNVLLVDDSIVRGTTSEQIIEMAREAGAKKVYLASAAPEIRFPNVYGIDMPSATELIAHG
REVDEIRQIIGADGLIFQDLNDLIDAVRAENPDIQQFECSVFNGVYVTKDVDQGYLDFLD
TLRNDDAKAVQRQNEVENLEMHNEG
References
External Links:
ResourceLink
Uniprot ID:P0AG16
Uniprot Name:PUR1_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:21239016
PDB ID:1ECG
Ecogene ID:EG10794
Ecocyc:EG10794
ColiBase:b2312
Kegg Gene:b2312
EchoBASE ID:EB0787
CCDB:PUR1_ECOLI
BacMap:16130247
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Krahn, J. M., Kim, J. H., Burns, M. R., Parry, R. J., Zalkin, H., Smith, J. L. (1997). "Coupled formation of an amidotransferase interdomain ammonia channel and a phosphoribosyltransferase active site." Biochemistry 36:11061-11068. Pubmed: 9333323
  • Muchmore, C. R., Krahn, J. M., Kim, J. H., Zalkin, H., Smith, J. L. (1998). "Crystal structure of glutamine phosphoribosylpyrophosphate amidotransferase from Escherichia coli." Protein Sci 7:39-51. Pubmed: 9514258
  • Nonet, M. L., Marvel, C. C., Tolan, D. R. (1987). "The hisT-purF region of the Escherichia coli K-12 chromosome. Identification of additional genes of the hisT and purF operons." J Biol Chem 262:12209-12217. Pubmed: 3040734
  • Sampei, G., Mizobuchi, K. (1988). "Nucleotide sequence of the Escherichia coli purF gene encoding amidophosphoribosyltransferase for de novo purine nucleotide synthesis." Nucleic Acids Res 16:8717. Pubmed: 3047685
  • Tso, J. Y., Hermodson, M. A., Zalkin, H. (1982). "Glutamine phosphoribosylpyrophosphate amidotransferase from cloned Escherichia coli purF. NH2-terminal amino acid sequence, identification of the glutamine site, and trace metal analysis." J Biol Chem 257:3532-3536. Pubmed: 7037784
  • Tso, J. Y., Zalkin, H., van Cleemput, M., Yanofsky, C., Smith, J. M. (1982). "Nucleotide sequence of Escherichia coli purF and deduced amino acid sequence of glutamine phosphoribosylpyrophosphate amidotransferase." J Biol Chem 257:3525-3531. Pubmed: 6277938
  • Yamamoto, Y., Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Itoh, T., Kimura, S., Kitagawa, M., Makino, K., Miki, T., Mitsuhashi, N., Mizobuchi, K., Mori, H., Nakade, S., Nakamura, Y., Nashimoto, H., Oshima, T., Oyama, S., Saito, N., Sampei, G., Satoh, Y., Sivasundaram, S., Tagami, H., Horiuchi, T., et, a. l. .. (1997). "Construction of a contiguous 874-kb sequence of the Escherichia coli -K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." DNA Res 4:91-113. Pubmed: 9205837
  • Zalkin, H. (1983). "Structure, function, and regulation of amidophosphoribosyltransferase from prokaryotes." Adv Enzyme Regul 21:225-237. Pubmed: 6443594